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Article

Voltage- and ATP-dependent structural rearrangements of the P2X2 receptor associated with the gating of the pore.

The Journal of physiology - 1 Nov 2014

Keceli Batu, Kubo Yoshihiro

Abstract excerpt

P2X2 is an extracellular ATP-gated cation channel which has a voltage-dependent gating property even though it lacks a canonical voltage sensor. It is a trimer in which each subunit has two transmembrane helices and a large extracellular domain. The three inter-subunit ATP binding sites are linked to the pore forming transmembrane (TM) domains by β-strands. We analysed structural rearrangements of the linker...

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Identifiers

PMID: 25172943
DOI: 10.1113/jphysiol.2014.278507
PMCID: PMC4253469

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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